ZN721_HUMAN - dbPTM
ZN721_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN721_HUMAN
UniProt AC Q8TF20
Protein Name Zinc finger protein 721
Gene Name ZNF721
Organism Homo sapiens (Human).
Sequence Length 911
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MCSHFTQDFLPVQGIEDSFHKLILRRYEKCGHDNLQLRKGCKSMNVCKVQKGVYNGINKCLSNTQSKIFQCNARVKVFSKFANSNKDKTRHTGEKHFKCNECGKSFQKFSDLTQHKGIHAGEKPYTCEERGKDFGWYTDLNQHKKIHTGEKPYKCEECGKAFNRSTNLTAHKRIHNREKAYTGEDRDRAFGWSTNLNEYKKIHTGDKPYKCKECGKAFMHSSHLNKHEKIHTGEKPYKCKECGKVISSSSSFAKHKRIHTGEKPFKCLECGKAFNISTTLTKHRRIHTGEKPYTCEVCGKAFRQSANLYVHRRIHTGEKPYTCGECGKTFRQSANLYVHRRIHTGEKPYKCEDCGKAFGRYTALNQHKKIHTGEKPYKCEECGKAFNSSTNLTAHKRIHTREKPYTCEDRGRAFGLSTNLNEYKKIHTGDKPYKCKECGKAFIHSLHLNKHEKIHTGKKPYKCKQCGKVITSSSSFAKHKRIHTGEKPFECLECGKAFTSSTTLTKHRRIHTGEKPYTCEVCGKAFRQSAILYVHRRIHTGEKPYTCEECGKTFRQSANLYVHRRIHTGEKPYKCEECGKAFGRYTDLNQHKKIHTGEKLYKCEECGKDFVWYTDLNQQKKIYTGEKPYKCEECGKAFAPSTDLNQHTKILTGEQSYKCEECGKAFGWSIALNQHKKIHTGEKPYKCEECGKAFSRSRNLTTHRRVHTREKPYKCEDRGRSFGWSTNLNEYKKIHTGDKLYKCKECGKVFKQSSHLNRHEKIHTGKKPYKCKECGKVITSSSSFAKHKRIHTGEKPFKCLECGKAFTSSTTLTKHRRIHTGEKPYTCEECGKAFRQSAILYVHRRIHTGEKPYTCGECGKTFRQSANLYAHKKIHTGEKPYTCGDCGKTFRQSANLYAHKKIHTGDKTIQV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
54PhosphorylationCKVQKGVYNGINKCL
CHHHCCHHCCHHHHH
19.1519690332
62PhosphorylationNGINKCLSNTQSKIF
CCHHHHHHCCCHHHH
47.5029083192
64PhosphorylationINKCLSNTQSKIFQC
HHHHHHCCCHHHHCC
30.7329083192
66PhosphorylationKCLSNTQSKIFQCNA
HHHHCCCHHHHCCCH
26.1929083192
92UbiquitinationNKDKTRHTGEKHFKC
CCCCCCCCCCCCEEE
43.6929967540
92PhosphorylationNKDKTRHTGEKHFKC
CCCCCCCCCCCCEEE
43.6923532336
132SumoylationYTCEERGKDFGWYTD
EEHHHCCCCCCCCCC
56.98-
135UbiquitinationEERGKDFGWYTDLNQ
HHCCCCCCCCCCHHH
26.9829967540
137PhosphorylationRGKDFGWYTDLNQHK
CCCCCCCCCCHHHCC
7.25-
144UbiquitinationYTDLNQHKKIHTGEK
CCCHHHCCCCCCCCC
43.5929967540
148PhosphorylationNQHKKIHTGEKPYKC
HHCCCCCCCCCCEEH
50.9729496963
153PhosphorylationIHTGEKPYKCEECGK
CCCCCCCEEHHHHHH
39.06-
154SumoylationHTGEKPYKCEECGKA
CCCCCCEEHHHHHHH
43.63-
154UbiquitinationHTGEKPYKCEECGKA
CCCCCCEEHHHHHHH
43.63-
194PhosphorylationDRAFGWSTNLNEYKK
HHCCCCCCCHHHHHC
36.90-
199PhosphorylationWSTNLNEYKKIHTGD
CCCCHHHHHCCCCCC
19.26-
204PhosphorylationNEYKKIHTGDKPYKC
HHHHCCCCCCCCCCC
51.0224719451
232PhosphorylationNKHEKIHTGEKPYKC
CCCCCCCCCCCCCCC
50.9729496963
237PhosphorylationIHTGEKPYKCKECGK
CCCCCCCCCCCCCCC
39.83-
249PhosphorylationCGKVISSSSSFAKHK
CCCEECCCCHHHHCC
24.18-
250PhosphorylationGKVISSSSSFAKHKR
CCEECCCCHHHHCCC
31.27-
251PhosphorylationKVISSSSSFAKHKRI
CEECCCCHHHHCCCC
31.04-
260PhosphorylationAKHKRIHTGEKPFKC
HHCCCCCCCCCCEEE
44.6718669648
266SumoylationHTGEKPFKCLECGKA
CCCCCCEEEECCCCE
46.57-
266UbiquitinationHTGEKPFKCLECGKA
CCCCCCEEEECCCCE
46.5729967540
278UbiquitinationGKAFNISTTLTKHRR
CCEEEEECCEECCCC
23.2521890473
288PhosphorylationTKHRRIHTGEKPYTC
ECCCCCCCCCCCEEE
44.6729083192
293PhosphorylationIHTGEKPYTCEVCGK
CCCCCCCEEEEECHH
34.7818083107
316PhosphorylationYVHRRIHTGEKPYTC
EEECCCCCCCCCEEC
44.6728111955
319UbiquitinationRRIHTGEKPYTCGEC
CCCCCCCCCEECCCC
44.67-
344PhosphorylationYVHRRIHTGEKPYKC
EEEEEECCCCCCEEC
44.6729496963
347UbiquitinationRRIHTGEKPYKCEDC
EEECCCCCCEECCCH
55.80-
350SumoylationHTGEKPYKCEDCGKA
CCCCCCEECCCHHHH
39.41-
350UbiquitinationHTGEKPYKCEDCGKA
CCCCCCEECCCHHHH
39.41-
372PhosphorylationNQHKKIHTGEKPYKC
HCCCCCCCCCCCEEH
50.9729496963
377PhosphorylationIHTGEKPYKCEECGK
CCCCCCCEEHHHHHH
39.06-
378SumoylationHTGEKPYKCEECGKA
CCCCCCEEHHHHHHC
43.63-
378UbiquitinationHTGEKPYKCEECGKA
CCCCCCEEHHHHHHC
43.63-
390PhosphorylationGKAFNSSTNLTAHKR
HHCCCCCCCCCCCCC
33.7824114839
393PhosphorylationFNSSTNLTAHKRIHT
CCCCCCCCCCCCCCC
28.8724114839
428PhosphorylationNEYKKIHTGDKPYKC
HHCCCCCCCCCCCCC
51.0224719451
478SumoylationTSSSSFAKHKRIHTG
ECCCHHHHCCCCCCC
47.88-
478SumoylationTSSSSFAKHKRIHTG
ECCCHHHHCCCCCCC
47.8828112733
490UbiquitinationHTGEKPFECLECGKA
CCCCCCEEEECCCCE
46.8829967540
499PhosphorylationLECGKAFTSSTTLTK
ECCCCEECCCCCEEE
26.99-
501PhosphorylationCGKAFTSSTTLTKHR
CCCEECCCCCEEECC
23.50-
502PhosphorylationGKAFTSSTTLTKHRR
CCEECCCCCEEECCC
26.1219413330
505PhosphorylationFTSSTTLTKHRRIHT
ECCCCCEEECCCCCC
23.7827762562
512PhosphorylationTKHRRIHTGEKPYTC
EECCCCCCCCCCEEE
44.6729083192
517PhosphorylationIHTGEKPYTCEVCGK
CCCCCCCEEEEECCH
34.7818083107
527MethylationEVCGKAFRQSAILYV
EECCHHHHHHEEEEE
34.1124384611
540PhosphorylationYVHRRIHTGEKPYTC
EEEEECCCCCCCEEH
44.6728111955
568PhosphorylationYVHRRIHTGEKPYKC
EEEEEECCCCCCEEH
44.6729496963
573PhosphorylationIHTGEKPYKCEECGK
ECCCCCCEEHHHHHH
39.06-
574UbiquitinationHTGEKPYKCEECGKA
CCCCCCEEHHHHHHH
43.63-
574SumoylationHTGEKPYKCEECGKA
CCCCCCEEHHHHHHH
43.63-
585PhosphorylationCGKAFGRYTDLNQHK
HHHHHCCCCCHHHCC
12.65-
596PhosphorylationNQHKKIHTGEKLYKC
HHCCCCCCCCCEEEC
50.97-
601PhosphorylationIHTGEKLYKCEECGK
CCCCCCEEECCHHCC
25.35-
602SumoylationHTGEKLYKCEECGKD
CCCCCEEECCHHCCC
45.68-
623PhosphorylationLNQQKKIYTGEKPYK
CCCCCCEECCCCCEE
19.99-
629PhosphorylationIYTGEKPYKCEECGK
EECCCCCEECCCCCC
39.06-
630SumoylationYTGEKPYKCEECGKA
ECCCCCEECCCCCCE
43.63-
649SumoylationTDLNQHTKILTGEQS
CCCCCCCCCCCCCCE
33.3328112733
658UbiquitinationLTGEQSYKCEECGKA
CCCCCEEECHHHHHH
40.18-
658SumoylationLTGEQSYKCEECGKA
CCCCCEEECHHHHHH
40.18-
680PhosphorylationNQHKKIHTGEKPYKC
CCCCCCCCCCCCEEC
50.9729496963
685PhosphorylationIHTGEKPYKCEECGK
CCCCCCCEECHHHHH
39.06-
686UbiquitinationHTGEKPYKCEECGKA
CCCCCCEECHHHHHH
43.63-
686SumoylationHTGEKPYKCEECGKA
CCCCCCEECHHHHHH
43.63-
721PhosphorylationKCEDRGRSFGWSTNL
ECCCCCCCCCCCCCH
30.8225332170
731PhosphorylationWSTNLNEYKKIHTGD
CCCCHHHCCCCCCCC
19.26-
736PhosphorylationNEYKKIHTGDKLYKC
HHCCCCCCCCCEEEH
51.0225332170
744UbiquitinationGDKLYKCKECGKVFK
CCCEEEHHHHHHHHH
52.4629967540
763UbiquitinationLNRHEKIHTGKKPYK
CCCCCCCCCCCCCCC
39.3729967540
786SumoylationTSSSSFAKHKRIHTG
ECCCHHHCCCCCCCC
47.8828112733
786SumoylationTSSSSFAKHKRIHTG
ECCCHHHCCCCCCCC
47.88-
792PhosphorylationAKHKRIHTGEKPFKC
HCCCCCCCCCCCEEE
44.6718669648
798UbiquitinationHTGEKPFKCLECGKA
CCCCCCEEEECCCCE
46.57-
798SumoylationHTGEKPFKCLECGKA
CCCCCCEEEECCCCE
46.57-
807PhosphorylationLECGKAFTSSTTLTK
ECCCCEECCCCCCEE
26.99-
809PhosphorylationCGKAFTSSTTLTKHR
CCCEECCCCCCEECC
23.50-
810UbiquitinationGKAFTSSTTLTKHRR
CCEECCCCCCEECCC
26.1221890473
810PhosphorylationGKAFTSSTTLTKHRR
CCEECCCCCCEECCC
26.1219413330
820PhosphorylationTKHRRIHTGEKPYTC
EECCCCCCCCCCCCH
44.6728111955
835MethylationEECGKAFRQSAILYV
HHHHHHHHHHHHHEE
34.1124384617
848PhosphorylationYVHRRIHTGEKPYTC
EEECCCCCCCCCEEC
44.6728111955
876PhosphorylationYAHKKIHTGEKPYTC
EEECEECCCCCCEEC
50.97-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of ZN721_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN721_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of ZN721_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN721_HUMAN !!

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN721_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP